Ontology highlight
ABSTRACT:
SUBMITTER: Piazzetta P
PROVIDER: S-EPMC6152773 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
Piazzetta Paolo P Marino Tiziana T Russo Nino N
Molecules (Basel, Switzerland) 20170618 6
In order to elucidate the elementary mechanism of the promiscuous esterase activity of human carbonic anhydrase (h-CA), we present an accurate theoretical investigation on the hydrolysis of fully-acetylated d-glucose functionalized as sulfamate. This h-CA's inhibitor is of potential relevance in cancer therapy. The study has been performed within the framework of three-layer ONIOM (QM-high:QM'-medium:MM-low) hybrid approach. The computations revealed that the hydrolysis process is not energetica ...[more]